Item Details

abstract

The sterile alpha motif (SAM) and histidine-aspartic acid (HD) domain containingprotein 1 (SAMHD1) has been implicated in multiple disease states including cancer, autoimmune disease, and viral infection. Early research into SAMHD1 identified the deoxynucleotide triphosphate (dNTP) triphosphohydrolase (dNTPase) activity that has positioned SAMHD1 as a central regulator of intracellular dNTP pools. As such, the field has centered around understanding the mechanism and regulation of SAMHD1 catalytic activity. However, SAMHD1 is emerging as a multifunctional enzyme with roles beyond dNTPase activity including nucleic acid binding and the DNA damage response. With the discovery of new, non-catalytic roles for SAMHD1, addressing the impact of these functions in the context of cancer, autoimmunity, and viral restriction is important.

subject

DNA Damage

DNA Repair

Protein Oxidation

SAMHD1

contributor

Simermeyer, Theresa Lynn (author)

Hollis, Thomas (committee chair)

Ornelles, David A (committee member)

Lyles, Douglas S (committee member)

Perrino, Fred W (committee member)

Poole, Leslie B (committee member)

date

2022-01-15T09:35:33Z (accessioned)

2021 (issued)

degree

Biochemistry and Molecular Biology (discipline)

2024-01-14 (liftdate)

embargo

2024-01-14 (terms)

identifier

http://hdl.handle.net/10339/99394 (uri)

language

en (iso)

publisher

Wake Forest University

title

OXIDATION REGULATES THE MULTIPLE FUNCTIONS OF SAMHD1

type

Dissertation